(1) The properties of monomeric phosphorylase B, formed with minimal structural alteration in low concentrations of propyl-urea, will be examined. (2) The physical properties and mechanism of auto-activation of purified phosphorylase kinase will be studied, with particular attention to structural changes occurring upon activation and the effects of cofactors. (3) The kinetics and mechanism of the enzymic phosphorylation of phosphorylase B by phosphorylase kinase will be studied. (4) The activation of phosphorylase kinase by purified cyclic AMP-dependent protein kinase will be studied, and the product of this activation will be compared with that of auto-activation. (5) The kinetics of binding of the activator analog epilon-AMP by phosphorylase B will examined, using a fluorescence stopped-flow technique. (6) The binding of the activator Ca ions by phosphorylase kinase will be studied, with particular attention to possible conformational changes and the effects of activation.